Bacterial expression systems have been utilized to produce large quantities of homogeneous proteins whose function may then be assayed and studied irrespective of the sequence of that protein or its abundance in its natural host. However, the bacterial expression process renders many proteins insoluble. Once a protein is rendered insoluble, the protein must be solubilized.
Certain methods have been developed to solubilize proteins which have been rendered insoluble by bacterial expression. However, the solubilization methods created heretofore necessarily entail denaturation of the protein. As a result, the protein must necessarily be renatured. This renaturation process may be costly and time consuming. In many instances, renaturation is not possible. Therefore, a need has arisen to create a method for solubilizing bacterially-expressed proteins which does not denature the proteins, and therefore eliminates the necessity to renature altogether.